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HEADER HYDROLASE 16-JUL-19 6KHL
TITLE LIPASE (BLOCKED FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUTIBACTERIUM ACNES HL110PA4;
SOURCE 3 ORGANISM_TAXID: 765080;
SOURCE 4 GENE: HMPREF9578_02569;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.KIM,A.R.KWON
REVDAT 1 22-JUL-20 6KHL 0
JRNL AUTH H.J.KIM,B.J.LEE,A.R.KWON
JRNL TITL CLOSED, BLOCKED, AND OPEN STATES OF LIPASE FROM TYPE II
JRNL TITL 2 CUTIBACTERIUM ACNES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 85381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4471
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5521
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.1550
REMARK 3 BIN FREE R VALUE SET COUNT : 263
REMARK 3 BIN FREE R VALUE : 0.1720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4709
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 704
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : -0.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.036
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4947 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4484 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6686 ; 1.852 ; 1.637
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10355 ; 1.638 ; 1.582
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 620 ; 6.475 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 269 ;31.390 ;22.045
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 729 ;11.928 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;17.658 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 621 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5617 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1068 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6KHL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89922
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (W/V) PEG 8K AND 0.1 M TRIS, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 47.23650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.82850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.23650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.82850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 312
REMARK 465 ILE A 313
REMARK 465 LYS A 314
REMARK 465 ARG A 315
REMARK 465 SER A 316
REMARK 465 ARG A 317
REMARK 465 MET B 1
REMARK 465 ARG B 311
REMARK 465 ARG B 312
REMARK 465 ILE B 313
REMARK 465 LYS B 314
REMARK 465 ARG B 315
REMARK 465 SER B 316
REMARK 465 ARG B 317
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 114 C04 DK0 A 401 1.61
REMARK 500 OG SER B 114 C04 DK0 B 401 1.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 40 -159.63 -126.55
REMARK 500 SER A 114 -115.16 58.65
REMARK 500 LEU A 131 90.82 -167.14
REMARK 500 THR A 148 -49.29 -138.28
REMARK 500 ALA A 162 61.53 -157.27
REMARK 500 ARG A 284 -145.22 -102.40
REMARK 500 GLU B 40 -159.60 -127.93
REMARK 500 PHE B 103 38.73 -141.98
REMARK 500 SER B 114 -114.10 54.87
REMARK 500 LEU B 131 99.08 -163.06
REMARK 500 THR B 148 -37.63 -138.09
REMARK 500 ALA B 162 58.58 -150.29
REMARK 500 ARG B 284 -131.13 -96.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK0 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK0 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 408
DBREF 6KHL A 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHL B 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
SEQRES 1 A 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 A 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 A 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 A 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 A 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 A 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 A 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 A 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 A 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 A 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 A 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 A 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 A 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 A 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 A 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 A 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 A 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 A 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 A 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 A 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 A 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 A 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 A 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 A 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 A 317 ILE LYS ARG SER ARG
SEQRES 1 B 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 B 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 B 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 B 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 B 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 B 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 B 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 B 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 B 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 B 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 B 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 B 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 B 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 B 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 B 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 B 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 B 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 B 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 B 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 B 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 B 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 B 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 B 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 B 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 B 317 ILE LYS ARG SER ARG
HET DK0 A 401 10
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET PEG A 406 7
HET PEG A 407 7
HET GOL A 408 6
HET GOL A 409 6
HET DK0 B 401 10
HET PEG B 402 7
HET PEG B 403 7
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HET GOL B 408 6
HETNAM DK0 (2~{R})-1-PHENYLPROPAN-2-OL
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 DK0 2(C9 H12 O)
FORMUL 4 GOL 11(C3 H8 O3)
FORMUL 8 PEG 4(C4 H10 O3)
FORMUL 20 HOH *704(H2 O)
HELIX 1 AA1 HIS A 41 ARG A 44 5 4
HELIX 2 AA2 TYR A 45 ALA A 55 1 11
HELIX 3 AA3 HIS A 67 GLY A 75 1 9
HELIX 4 AA4 ASN A 83 GLN A 98 1 16
HELIX 5 AA5 SER A 114 THR A 125 1 12
HELIX 6 AA6 PRO A 143 THR A 148 1 6
HELIX 7 AA7 ASP A 151 ALA A 162 1 12
HELIX 8 AA8 PRO A 168 PHE A 176 1 9
HELIX 9 AA9 THR A 190 ALA A 194 5 5
HELIX 10 AB1 SER A 196 ASP A 206 1 11
HELIX 11 AB2 SER A 216 GLY A 232 1 17
HELIX 12 AB3 GLY A 232 MET A 239 1 8
HELIX 13 AB4 ASP A 252 ASP A 256 5 5
HELIX 14 AB5 GLY A 258 ASP A 271 1 14
HELIX 15 AB6 SER A 293 ARG A 311 1 19
HELIX 16 AB7 HIS B 41 ARG B 44 5 4
HELIX 17 AB8 TYR B 45 ALA B 55 1 11
HELIX 18 AB9 HIS B 67 GLY B 75 1 9
HELIX 19 AC1 ASN B 83 GLN B 98 1 16
HELIX 20 AC2 SER B 114 THR B 125 1 12
HELIX 21 AC3 PRO B 143 THR B 148 1 6
HELIX 22 AC4 ASP B 151 ALA B 162 1 12
HELIX 23 AC5 PRO B 168 PHE B 176 1 9
HELIX 24 AC6 SER B 184 GLY B 188 5 5
HELIX 25 AC7 THR B 190 ALA B 194 5 5
HELIX 26 AC8 SER B 196 GLY B 204 1 9
HELIX 27 AC9 SER B 216 GLY B 232 1 17
HELIX 28 AD1 GLY B 232 MET B 239 1 8
HELIX 29 AD2 ASP B 252 ASP B 256 5 5
HELIX 30 AD3 GLY B 258 ASP B 271 1 14
HELIX 31 AD4 SER B 293 ASN B 310 1 18
SHEET 1 AA1 8 LEU A 3 THR A 9 0
SHEET 2 AA1 8 ALA A 16 TYR A 22 -1 O ILE A 17 N PHE A 8
SHEET 3 AA1 8 PHE A 57 ASP A 63 -1 O VAL A 59 N TYR A 22
SHEET 4 AA1 8 ALA A 30 ILE A 35 1 N VAL A 32 O VAL A 58
SHEET 5 AA1 8 TRP A 108 HIS A 113 1 O PHE A 111 N GLN A 33
SHEET 6 AA1 8 GLY A 133 CYS A 137 1 O ALA A 135 N VAL A 110
SHEET 7 AA1 8 ILE A 244 GLY A 249 1 O VAL A 245 N LEU A 136
SHEET 8 AA1 8 VAL A 275 TYR A 280 1 O TYR A 280 N ALA A 248
SHEET 1 AA2 8 LEU B 3 THR B 9 0
SHEET 2 AA2 8 ALA B 16 TYR B 22 -1 O ILE B 17 N PHE B 8
SHEET 3 AA2 8 PHE B 57 ASP B 63 -1 O VAL B 59 N TYR B 22
SHEET 4 AA2 8 ALA B 30 ILE B 35 1 N VAL B 32 O VAL B 58
SHEET 5 AA2 8 TRP B 108 HIS B 113 1 O PHE B 111 N GLN B 33
SHEET 6 AA2 8 GLY B 133 CYS B 137 1 O ALA B 135 N VAL B 110
SHEET 7 AA2 8 ILE B 244 GLY B 249 1 O PHE B 247 N LEU B 136
SHEET 8 AA2 8 VAL B 275 TYR B 280 1 O TYR B 280 N ALA B 248
SITE 1 AC1 10 LEU A 38 SER A 114 TRP A 115 VAL A 140
SITE 2 AC1 10 PHE A 176 PHE A 179 TRP A 192 PHE A 211
SITE 3 AC1 10 HIS A 285 GOL A 409
SITE 1 AC2 5 GLN A 142 ASN A 231 TYR A 236 ARG A 267
SITE 2 AC2 5 HOH A 543
SITE 1 AC3 5 ARG A 69 HOH A 692 HOH A 695 ARG B 69
SITE 2 AC3 5 GLN B 73
SITE 1 AC4 8 PHE A 179 PRO A 189 TRP A 192 GOL A 408
SITE 2 AC4 8 HOH A 506 HOH A 597 HOH A 673 HOH A 687
SITE 1 AC5 5 ASN A 210 PHE A 211 ALA A 213 PRO A 214
SITE 2 AC5 5 HOH A 711
SITE 1 AC6 9 ARG A 44 ASP A 202 ASP A 206 ASN A 289
SITE 2 AC6 9 HOH A 583 HOH A 652 HOH A 793 ALA B 2
SITE 3 AC6 9 LEU B 3
SITE 1 AC7 12 VAL A 76 TRP A 77 ALA A 78 ASP A 79
SITE 2 AC7 12 THR A 164 ASP A 165 PRO A 166 PRO A 214
SITE 3 AC7 12 MET A 215 SER A 216 HOH A 502 HOH A 791
SITE 1 AC8 8 GLY A 39 PHE A 211 GLY A 212 ALA A 213
SITE 2 AC8 8 GOL A 404 HOH A 536 HOH A 597 HOH A 742
SITE 1 AC9 8 LEU A 38 HIS A 113 SER A 114 HIS A 203
SITE 2 AC9 8 PHE A 211 HIS A 285 GLU A 286 DK0 A 401
SITE 1 AD1 9 LEU B 38 SER B 114 TRP B 115 VAL B 140
SITE 2 AD1 9 PHE B 176 TRP B 192 PHE B 211 HIS B 285
SITE 3 AD1 9 GOL B 406
SITE 1 AD2 6 ASP B 104 LEU B 106 ASP B 132 VAL B 308
SITE 2 AD2 6 HOH B 717 HOH B 951
SITE 1 AD3 8 ALA A 2 ARG B 44 ASP B 202 ASP B 206
SITE 2 AD3 8 ASN B 289 HOH B 756 HOH B 773 HOH B 967
SITE 1 AD4 6 PRO B 143 ARG B 144 PRO B 253 ASP B 256
SITE 2 AD4 6 PHE B 257 HOH B 708
SITE 1 AD5 7 GLY B 39 PHE B 211 GLY B 212 ALA B 213
SITE 2 AD5 7 GOL B 408 HOH B 735 HOH B 877
SITE 1 AD6 9 GLY B 37 LEU B 38 HIS B 113 SER B 114
SITE 2 AD6 9 HIS B 203 PHE B 211 HIS B 285 GLU B 286
SITE 3 AD6 9 DK0 B 401
SITE 1 AD7 5 MET A 72 PHE A 208 HOH A 678 GLN B 4
SITE 2 AD7 5 GLU B 5
SITE 1 AD8 6 PHE B 176 PRO B 189 TRP B 192 GOL B 405
SITE 2 AD8 6 HOH B 711 HOH B 754
CRYST1 94.473 129.657 55.464 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010585 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018030 0.00000
TER 2364 ARG A 311
TER 4714 ASN B 310
MASTER 371 0 17 31 16 0 39 6 5527 2 114 50
END |